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A9I4U2 (MRAY_BORPD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phospho-N-acetylmuramoyl-pentapeptide-transferase
EC=2.7.8.13
Alternative name(s):
UDP-MurNAc-pentapeptide phosphotransferase
Gene names
Name:mraY
Ordered Locus Names:Bpet0694
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan By similarity. HAMAP MF_00038

Catalytic activity

UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. HAMAP MF_00038

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00038

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_00038.

Sequence similarities

Belongs to the glycosyltransferase 4 family. MraY subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 389389Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP MF_00038
PRO_1000090596

Regions

Transmembrane21 – 4121Helical; Potential
Transmembrane71 – 9121Helical; Potential
Transmembrane97 – 11721Helical; Potential
Transmembrane134 – 15421Helical; Potential
Transmembrane167 – 18721Helical; Potential
Transmembrane190 – 21021Helical; Potential
Transmembrane222 – 24221Helical; Potential
Transmembrane259 – 27921Helical; Potential
Transmembrane286 – 30621Helical; Potential
Transmembrane311 – 33121Helical; Potential
Transmembrane366 – 38621Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
A9I4U2 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 3DFA265111049F4C

FASTA38942,715
        10         20         30         40         50         60 
MLLEIARWLS DDVRAIGVLE YITMRAVLAC ATALLIGLVA GPRVIRKLTE MKIGQAVRAY 

        70         80         90        100        110        120 
GPESHLVKTG TPTMGGALIL IAVAISTLLW ADWTNRFVWV VLLVTFGFGW IGWMDDYRKV 

       130        140        150        160        170        180 
VYRDPEGMPA RQKFFWQATI GLVAAVYLAF AVSAPANTEL WPLFKAWVSS GFAMPLPTRA 

       190        200        210        220        230        240 
DLIVPFFKSV SYPLGVLGFV ALTWAVIVGT SNAVNLTDGL DGLAIMPTVM VGSALGIFAY 

       250        260        270        280        290        300 
VVGRVDYSKY LLFPYIPGAA ELMVLCAAIA GAGLAFLWFN AYPAQVFMGD VGALALGGAL 

       310        320        330        340        350        360 
GTIAVIVRQE IVLFIMGGVF VVETLSVMMQ VTWFKYTKRK YGQGRRIFRM APLHHHFEVG 

       370        380 
GWKETQVVVR FWIISMMLVL IGLSTLKLR

« Hide

References

[1]"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae."
Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. expand/collapse author list , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.
BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM902716 Genomic DNA. Translation: CAP41026.1.
RefSeqYP_001629297.1. NC_010170.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA9I4U2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5819507.
GenomeReviewsGene locus Bpet0694 in contig AM902716_GR.
KEGGbpt:Bpet0694.
PATRIC21162855. VBIBorPet31633_0700.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG708263.
OMARFWIISM.
ProtClustDBPRK00108.

Enzyme and pathway databases

BioCycBPET94624:BPET0694-MONOMER.

Family and domain databases

HAMAPMF_00038. MraY.
[Tree]
InterProIPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
[Graphical view]
KOK01000.
PANTHERPTHR22926. Glyco_trans_4. 1 hit.
PTHR22926:SF3. PNAcPpept_trans. 1 hit.
PfamPF00953. Glycos_transf_4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00445. MraY. 1 hit.
PROSITEPS01347. MRAY_1. 1 hit.
PS01348. MRAY_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMRAY_BORPD
AccessionPrimary (citable) accession number: A9I4U2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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